ArticleNature communications2014
Constitutive phospholipid scramblase activity of a G protein-coupled receptor.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
81 citing papers in PubMed, 127 citations in OpenAlex.
- Ultra-slow release of hydrophilic drugs via multilamellar-multivesicular liposomes formed by unsaturated phospholipids.Nature biomedical engineering · 2026Article
- A single-vesicle fluorescence microscopy platform to quantify phospholipid scrambling.Nature structural & molecular biology · 2026Article
- An ER-IMC bridge protein TgVPS13A and an IMC-resident scramblase TgDAT1 drive daughter budding in Toxoplasma gondii.PLoS pathogens · 2026Article
- Crystallographic data for Pyrococcus furiosus dolichylphosphate mannose synthase suggest that the enzyme could flip its glycolipid product.Scientific reports · 2026Article
- An artificial cell capable of signal transduction mediated by ADRB2 for the regulation of glycogenolysis.Nature communications · 2026Article
- Article
- A single vesicle fluorescence microscopy platform to quantify phospholipid scrambling.bioRxiv : the preprint server for biology · 2025Article
- Ist2 promotes lipid transfer by Osh6 via its membrane tethering and lipid scramblase activities.Science advances · 2025Article
- Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025Article
- Groove architecture controls lipid scrambling in simulations of protein and model systems.bioRxiv : the preprint server for biology · 2025Article
- MprF fromScience advances · 2025Article
- One-Pot Reconstitution of GPCRs into Unilamellar Vesicles for Fluorescence-Based Phospholipid Scramblase Activity Assay.Methods in molecular biology (Clifton, N.J.) · 2025Article
- In or out of the groove? Mechanisms of lipid scrambling by TMEM16 proteins.Cell calcium · 2024Review
- A cholesterol switch controls phospholipid scrambling by G protein-coupled receptors.The Journal of biological chemistry · 2024Article
- Subcellular distribution of membrane lipids revealed by freeze-fracture electron microscopy.Anatomical science international · 2024Review
- Article
- Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase.Nature communications · 2023Article
- Lactose Permease Scrambles Phospholipids.Biology · 2023Article
- Reconstitution of ATP-dependent lipid transporters: gaining insight into molecular characteristics, regulation, and mechanisms.Bioscience reports · 2023Review
- Antiviral HIV-1 SERINC restriction factors disrupt virus membrane asymmetry.Nature communications · 2023Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Opsin, the rhodopsin apoprotein, was recently shown to be an ATP-independent flippase (or scramblase) that equilibrates phospholipids across photoreceptor disc membranes in mammalian retina, a process required for disc homoeostasis. Here we show that scrambling is a constitutive activity of rhodopsin, distinct from its light-sensing function. Upon reconstitution into vesicles, discrete conformational states of the protein (rhodopsin, a metarhodopsin II-mimic, and two forms of opsin) facilitated rapid (>10,000 phospholipids per protein per second) scrambling of phospholipid probes. Our results indicate that the large conformational changes involved in converting rhodopsin to metarhodopsin II are not required for scrambling, and that the lipid translocation pathway either lies near the protein surface or involves membrane packing defects in the vicinity of the protein. In addition, we demonstrate that β2-adrenergic and adenosine A2A receptors scramble lipids, suggesting that rhodopsin-like G protein-coupled receptors may play an unexpected moonlighting role in re-modelling cell membranes.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.